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7vop

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'''Unreleased structure'''
 
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The entry 7vop is ON HOLD until Paper Publication
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==Cryo-EM structure of Xenopus laevis nuclear pore complex cytoplasmic ring subunit==
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<StructureSection load='7vop' size='340' side='right'caption='[[7vop]], [[Resolution|resolution]] 8.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7vop]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VOP FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7vop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vop OCA], [https://pdbe.org/7vop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vop RCSB], [https://www.ebi.ac.uk/pdbsum/7vop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vop ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/Q4KLQ6_XENLA Q4KLQ6_XENLA]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 A resolution cryo-electron microscopic (cryo-EM) structure of the outer rings containing nuclear ring (NR) and cytoplasmic ring (CR) from the Xenopus laevis NPC, with local resolutions reaching 4.9 A. With the aid of AlphaFold2, we managed to build a pseudoatomic model of the outer rings, including the Y complexes and flanking components. In this most comprehensive and accurate model of outer rings to date, the almost complete Y complex structure exhibits much tighter interaction in the hub region. In addition to two copies of Y complexes, each asymmetric subunit in CR contains five copies of Nup358, two copies of the Nup214 complex, two copies of Nup205 and one copy of newly identified Nup93, while that in NR contains one copy of Nup205, one copy of ELYS and one copy of Nup93. These in-depth structural features represent a great advance in understanding the assembly of NPCs.
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Authors: Tai, L., Zhu, Y., Sun, F.
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8 A structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.,Tai L, Zhu Y, Ren H, Huang X, Zhang C, Sun F Protein Cell. 2022 Oct;13(10):760-777. doi: 10.1007/s13238-021-00895-y. Epub 2022, Jan 11. PMID:35015240<ref>PMID:35015240</ref>
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Description: Cryo-EM structure of Xenopus laevis nuclear pore complex cytoplasmic ring subunit
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Tai, L]]
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<div class="pdbe-citations 7vop" style="background-color:#fffaf0;"></div>
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[[Category: Zhu, Y]]
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== References ==
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[[Category: Sun, F]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Xenopus laevis]]
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[[Category: Sun F]]
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[[Category: Tai L]]
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[[Category: Zhu Y]]

Current revision

Cryo-EM structure of Xenopus laevis nuclear pore complex cytoplasmic ring subunit

PDB ID 7vop

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